The synovial proteome: analysis of fibroblast-like synoviocytes
dc.contributor.author | Dasuri, Kumar | |
dc.contributor.author | Antonovici, Mihaela | |
dc.contributor.author | Chen, Keding | |
dc.contributor.author | Wong, Ken | |
dc.contributor.author | Standing, Kenneth | |
dc.contributor.author | Ens, Werner | |
dc.contributor.author | El-Gabalawy, Hani | |
dc.contributor.author | Wilkins, John A | |
dc.date.accessioned | 2015-11-16T18:15:22Z | |
dc.date.available | 2015-11-16T18:15:22Z | |
dc.date.issued | 2004-02-16 | |
dc.date.updated | 2015-11-14T07:03:07Z | |
dc.description.abstract | Abstract The present studies were initiated to determine the protein expression patterns of fibroblast-like synovial (FLS) cells derived from the synovia of rheumatoid arthritis patients. The cellular proteins were separated by two-dimensional polyacrylamide gel electrophoresis and the in-gel digested proteins were analyzed by matrix-assisted laser desorption ionization mass spectrometry. A total of 368 spots were examined and 254 identifications were made. The studies identified a number of proteins that have been implicated in the normal or pathological FLS function (e.g. uridine diphosphoglucose dehydrogenase, galectin 1 and galectin 3) or that have been characterized as potential autoantigens in rheumatoid arthritis (e.g. BiP, colligin, HC gp-39). A novel uncharacterized protein product of chromosome 19 open reading frame 10 was also detected as an apparently major component of FLS cells. These results demonstrate the utility of high-content proteomic approaches in the analysis of FLS composition. | |
dc.identifier.citation | Arthritis Res Ther. 2004 Feb 16;6(2):R161 | |
dc.identifier.uri | http://dx.doi.org/10.1186/ar1153 | |
dc.identifier.uri | http://hdl.handle.net/1993/30934 | |
dc.language.rfc3066 | en | |
dc.rights | open access | en_US |
dc.rights.holder | Dasuri et al. | |
dc.title | The synovial proteome: analysis of fibroblast-like synoviocytes | |
dc.type | Journal Article |